Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

MATRIN3 deficiency leads to cGAS-STING activation (NanoString)

ABSTRACT: To investigate the role of Matrin 3 (MATR3) in innate immune response, we analyzed and compared MATR3 KO clones versus wildtype HAP1 cells.

ORGANISM(S): Homo sapiens

PROVIDER: GSE216829 | GEO | 2024/05/15

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Similar Datasets

MATRIN3 deficiency leads to cGAS-STING activation (MinION RNA-Seq)

Project description:To investigate the role of Matrin 3 (MATR3) in innate immune response we analyzed and compared MATR3 KO Clones versus wildtype HAP1 cells.

2024-05-15 | GSE216826 | GEO

MATRIN3 deficiency leads to cGAS-STING activation (Illumina RNA-Seq)

Project description:To investigate the role of Matrin 3 (MATR3) in the innate immune response we analyzed and compared MATR3 KO Clones versus wildtype HAP1 cells.

2024-05-15 | GSE216825 | GEO

MATRIN3 deficiency leads to cGAS-STING activation

Project description:To determine the direct targets of MATR3 in human HAP1 cells, we performed PAR-CLIP.

2024-05-15 | GSE262647 | GEO

MATRIN3 deficiency leads to cGAS-STING activation

Project description:This SuperSeries is composed of the SubSeries listed below.

2024-05-15 | GSE216830 | GEO

ALS Associated Mutations in Matrin 3 Alter Protein-Protein Interactions and Impede mRNA Nuclear Export

Project description:Mutations in Matrin 3 have recently been linked to ALS, though the mechanism of disease in these patients is still unknown. To define the protein interactome of wild-type and ALS-linked MATR3 mutations, we performed immunoprecipitation followed by mass spectrometry experiments in NSC-34 cells expressing human wild-type or mutant Matrin 3. Gene ontology analysis identified a novel role for Matrin in mRNA transport centered around proteins in the TRanscription and EXport (TREX) complex, known to function in mRNA biogenesis and nuclear export. ALS-linked mutations in Matrin 3 led to its re-distribution within the nucleus, decreased co-localization with endogenous Matrin 3 and increased co-localization with TREX components. Expression of disease-causing Matrin 3 mutations led to nuclear mRNA export defects of both global mRNA and the mRNA of ALS linked proteins TDP-43 and FUS. Our findings demonstrate the first pathogenic mechanism attributable to MATR3 mutations and further link cellular transport defects to ALS.

2017-11-15 | PXD007710 | Pride

Overlapping Splicing Regulatory Networks of the Nuclear Matrix Protein Matrin3 and PTB

Project description:Transcription and alternative splicing profiling in control and Matr3 siRNA treated HeLa S3 cells.

2014-11-27 | E-MTAB-3092 | biostudies-arrayexpress

CLIP-Seq of H. sapiens HeLa cells to investigate transcriptome-wide mapping of Matrin3

Project description:Matr3 iCLIP with 4thio-uridine labelling in HeLa cells

2014-12-01 | E-MTAB-3107 | biostudies-arrayexpress

STAG2 deficiency induces interferon responses via cGAS-STING pathway and restricts virus infection.

Project description:Cohesin is a multi-subunit nuclear protein complex that coordinates sister chromatid separation during cell division. Highly frequent somatic mutations in genes encoding core cohesin subunits have been reported in multiple cancer types. Here, using a genome-wide CRISPR-Cas9 screening approach to identify host dependency factors and novel innate immune regulators of rotavirus (RV) infection, we demonstrate that the loss of STAG2, an important component of the cohesin complex, confers resistance to RV replication in cell culture and human intestinal enteroids. Mechanistically, STAG2 deficiency results in spontaneous genomic DNA damage and robust interferon (IFN) expression via the cGAS-STING cytosolic DNA-sensing pathway. The resultant activation of JAK-STAT signaling and IFN-stimulated gene (ISG) expression broadly protects against virus infections, including RVs. Our work highlights a previously undocumented role of the cohesin complex in regulating IFN homeostasis and identifies new therapeutic avenues for manipulating the innate immunity.

| S-EPMC5902600 | biostudies-literature

MLH1 Deficiency-Triggered DNA Hyperexcision by Exonuclease 1 Activates the cGAS-STING Pathway.

Project description:Tumors with defective mismatch repair (dMMR) are responsive to immunotherapy because of dMMR-induced neoantigens and activation of the cGAS-STING pathway. While neoantigens result from the hypermutable nature of dMMR, it is unknown how dMMR activates the cGAS-STING pathway. We show here that loss of the MutLα subunit MLH1, whose defect is responsible for ~50% of dMMR cancers, results in loss of MutLα-specific regulation of exonuclease 1 (Exo1) during DNA repair. This leads to unrestrained DNA excision by Exo1, which causes increased single-strand DNA formation, RPA exhaustion, DNA breaks, and aberrant DNA repair intermediates. Ultimately, this generates chromosomal abnormalities and the release of nuclear DNA into the cytoplasm, activating the cGAS-STING pathway. In this study, we discovered a hitherto unknown MMR mechanism that modulates genome stability and has implications for cancer therapy.

| S-EPMC8666006 | biostudies-literature

Protein interaction networks for Matrin 3 encoding mutations

Project description:To understand how mutations in Matrin 3 (MATR3) cause amyotrophic lateral sclerosis (ALS) and distal myopathy, we used transcriptome and interactome analysis. We found over-expression of wild-type (WT) or F115C mutant MATR3 had little impact on gene expression in neuroglia cells. We identified ~123 proteins that bound MATR3, with proteins associated with stress granules and RNA processing/splicing being prominent. The interactome of myopathic S85C and ALS-variant F115C MATR3 were virtually identical to WT protein. Deletion of RNA recognition motif (RRM1) or Zn finger motifs (ZnF1 or ZnF2) diminished the binding of a subset of MATR3 interacting proteins. Remarkably, deletion of the RRM2 motif caused enhanced binding of >100 hundred proteins. In live cells, MATR3 lacking RRM2 (ΔRRM2) formed intranuclear spherical structures that fused over time into large structures. Our findings in the cell models used here suggest that MATR3 with disease-causing mutations is not dramatically different from WT protein in modulating gene regulation or in binding to normal interacting partners. The intra-nuclear localization and interaction network of MATR3 is strongly modulated by its RRM2 domain.

2018-08-03 | PXD008896 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data